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Disordered N-terminal residues affect the folding thermodynamics and kinetics of maltose binding protein

Ganesh, C and Banerjee, Antara and Shah, Aseema and Varadarajan, Raghavan (1999) Disordered N-terminal residues affect the folding thermodynamics and kinetics of maltose binding protein. In: FEBS Letters, 454 (3). pp. 307-311.

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Abstract

Maltose binding protein (MBP) exhibits a slow phase of folding at pH 7.4, 298 K. The kinetics of this phase has been characterized as a function of denaturant concentration and temperature. Denaturant double-jump experiments and the activation energy for folding indicate that the slow phase involves processes other than proline isomerization. Although the first five N-terminal residues are disordered in the MBP crystal structure, mutations in this region slow down folding and destabilize the native structure. This is the first report showing that disordered N-terminal residues can affect folding kinetics and stability.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Federation of European Biochemical Societies.
Keywords: Folding;Kinetics;Stability;Maltose binding protein;Double jump;Mass spectrometry
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 16 Oct 2007
Last Modified: 19 Sep 2010 04:40
URI: http://eprints.iisc.ernet.in/id/eprint/12119

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